Inhibin A ELISA

Inhibins are heterodimeric protein hormones secreted by granulosa cells of the ovary in the female and Sertoli cells of the testis in the male. They selectively suppress the secretion of pituitary follicle stimulating hormone (FSH) and also have local paracrine actions in the gonads. The fully processed form of the inhibin molecule has a molecular weight of approximately 32 kD and consists of the two distinct chains (α and β), linked by disulfide bridges. Higher molecular weight forms, with precursor forms of the α-subunit, also occur in follicular fluid and serum. In addition, free α-subunit forms, unassociated with a β-subunit, and lacking inhibin bioactivity, are also present. Inhibin A consists of an α-subunit and βA-subunit. Measurements of Inhibin A are shown to be useful in studying its role in human reproductive physiology.

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